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Immunofluorescence analysis of HSP70 was done on 70% confluent log phase HeLa. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.25% Triton™ X-100 for 10 minutes, and blocked with 5% BSA for 1 hour at room temperature. The cells were labeled with HSP70 Mouse monoclonal Antibody (333800) at 2µg/mL in 1% BSA and incubated for 3 hours at room temperature and then labeled with Alexa Flour 488 Rabbit Anti-Mouse IgG Secondary Antibody (A11059) at a dilution of 1:400 for 30 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant DAPI (S36938). F-actin (Panel c: red) was stained with Alexa Fluor 594 Phalloidin (A12381). Panel d is a merged image showing cytoplasmic localization. Panel e shows no primary antibody control. The images were captured at 20X magnification.
|Tested species reactivity||Human, Rat|
|Published species reactivity||Rat|
|Host / Isotype||Mouse / IgM|
|Immunogen||This antibody was prepared against full-length human hsp70 protein.|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay Dependent|
|Flow Cytometry (Flow)||1:100-1:500|
|Immunohistochemistry (Paraffin) (IHC (P))||1:20-1:200|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat. HSP90 is a 90 kDa protein that is induced under stress conditions, but is also one of the most abundant cellular proteins found under non-stress conditions. HSP90 has been found to be associated with a number of other intracellular proteins, including steroid receptors, actin, tubulin, aryl hydrocarbon (Ah) receptor, and some kinases. Studies have shown that murine HSP90 exists as two forms, HSP84 and HSP86, coded by related but separate genes, with 86% amino acid sequence conservation. These forms are analogous to the two forms of human HSP90, HSP89 alpha and HSP89 beta. In an unstressed mouse fibroblast, the basal level of HSP84 is found to be double that of HSP86. However, after heat shock, HSP86 shows a greater increase. Studies also suggest that upon cellular differentiation, the level of HSP86, but not HSP84, decreases. HSP84 and HSP86, which may be subject to estrogenic regulation, have been found as components of the non-DNA binding form of mouse glucocorticoid receptor, but dissociated from the transformed DNA-binding form.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
|Rat||Not Cited||Tapered progesterone withdrawal promotes long-term recovery following brain trauma.||Cutler SM,Vanlandingham JW,Stein DG||Experimental neurology (200:378)||2006|
dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1B; Heat shock 70 kDa protein 2; heat shock 70kD protein 1A; heat shock 70kDa protein 1A; heat shock protein 70-1; heat shock-induced protein; HSP70-1; HSP70-1/HSP70-2; HSP70-2; HSP70.1/2; HSP70.1/HSP70.2; HSPA1; HSPA1A; HSPA1B; Hspa70; HSX70
HEL-S-103; HSP70-1; HSP70-1A; Hsp70-2; HSP70.1; HSP70I; HSP72; HSPA1; HSPA1A; HSPA1B; Hspa2; HSX70